ID N2BUR4_9ACTN Unreviewed; 788 AA.
AC N2BUR4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EMZ42250.1};
GN ORFNames=HMPREF1091_01224 {ECO:0000313|EMBL:EMZ42250.1};
OS Atopobium minutum 10063974.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Atopobium.
OX NCBI_TaxID=997872 {ECO:0000313|EMBL:EMZ42250.1, ECO:0000313|Proteomes:UP000012651};
RN [1] {ECO:0000313|EMBL:EMZ42250.1, ECO:0000313|Proteomes:UP000012651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10063974 {ECO:0000313|EMBL:EMZ42250.1,
RC ECO:0000313|Proteomes:UP000012651};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Lambert T., Marvaud J.-C.,
RA Courvalin P., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Atopobium minutum 10063974.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMZ42250.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGXC01000002; EMZ42250.1; -; Genomic_DNA.
DR RefSeq; WP_002563969.1; NZ_KB822533.1.
DR AlphaFoldDB; N2BUR4; -.
DR PATRIC; fig|997872.3.peg.1231; -.
DR HOGENOM; CLU_012300_3_0_11; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000012651; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR NCBIfam; TIGR00691; spoT_relA; 1.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF19296; RelA_AH_RIS; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000012651};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 71..171
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 422..483
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 703..777
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 788 AA; 87949 MW; 645E5BA44A8842C2 CRC64;
MTQETSAGKG ITEEGLFVPV TDEIPEADNY SLLLRTCGQY LNEEDLQLVK DAYTFAARFH
GNQRRRSGEP YINHPVEVAF ILADKLHMDK DVICTALLHD TVEDTTATLN DIAFQFGETV
AELVDGVTKL TSIEVDSMDE KQALNLRKMF LAMSKDIRVV IIKLADRLHN MRTLASLPPH
RRIFKAKETM DVYAPLADRL GISSFKWELE DLSFFYLYTD EYTRIARMVQ DSHEARERET
NATIKVLSDE IAKTGITGLQ ITGRPKHLWS IYQKMKRKDK QFSDIYDLIA LRVIAQSVSD
CYSILGSVHS LWHPLPGRFK DYIATPKPNG YSSLHTTVVG PDARPIEIQI RTYEMHEQAE
YGIAAHWLYK RSGNSLGDRS HVDKSVDSQI SWIRRSLDWA AEADIDDAHE YLDSLRVDLY
EDEIFVFTPK GEVMSLRAGA TPLDFAYAVH TEVGNHCVGA KVNGSVVPLT YSLEIGDRVE
ILTNKNSKPS RDWIALVRTP SARAKIRKYF STASKSDDAE AGRSELAREL RKRGFGISNA
RTTKAINRVY PQYDLHTADD LFAAIGTSKL TAKSVANRVE AVLKEGSPEQ LAEAAKAAKE
QARKKEAMED DKPLKLAKPQ TREQRKKRAN CGVVVKGDSD LLVHLSKCCN PVAGDQIIGF
ITRGRGVSVH RANCPNVSDL MRHPERMIDV EWDTSGATEF QVEIVVAATD RIGLLKDVTI
VLDAVGANIL SAATQTSKTG AARLRFLLSI SDASILNPLL TAVGRVSGVY DARRILPGEG
SKQLKRRL
//
